| Tag | Content |
|---|
| CPLM ID | CPLM-002520 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | tRNA pseudouridine synthase A |
Protein Synonyms/Alias | tRNA pseudouridine(38-40) synthase; tRNA pseudouridylate synthase I; PSU-I; tRNA-uridine isomerase I |
Gene Name | truA |
Gene Synonyms/Alias | asuC; hisT; leuK; b2318; JW2315 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 38 | EVRSVQEKLEKALSQ | acetylation | [1] | | 41 | SVQEKLEKALSQVAN | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. |
Sequence Annotation | REGION 107 111 RNA binding.
REGION 168 172 Interaction with tRNA.
ACT_SITE 60 60 Nucleophile.
BINDING 118 118 Substrate. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Isomerase; Reference proteome; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 270 AA |
Protein Sequence | MSDQQQPPVY KIALGIEYDG SKYYGWQRQN EVRSVQEKLE KALSQVANEP ITVFCAGRTD 60
AGVHGTGQVV HFETTALRKD AAWTLGVNAN LPGDIAVRWV KTVPDDFHAR FSATARRYRY 120
IIYNHRLRPA VLSKGVTHFY EPLDAERMHR AAQCLLGEND FTSFRAVQCQ SRTPWRNVMH 180
INVTRHGPYV VVDIKANAFV HHMVRNIVGS LMEVGAHNQP ESWIAELLAA KDRTLAAATA 240
KAEGLYLVAV DYPDRYDLPK PPMGPLFLAD 270 |
Gene Ontology | GO:0009982; F:pseudouridine synthase activity; IDA:EcoCyc. GO:0000049; F:tRNA binding; IDA:EcoCyc. GO:0031119; P:tRNA pseudouridine synthesis; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |